DsRed-mediated oligomerization stabilizes HMGB1 on chromatin in vivo and on DNA in vitro.

Abstract:

:High-mobility group box-1 (HMGB1) is remarkably mobile in living cells, which reflects its ability to interact only transiently with both DNA and protein. This property is likely essential for HMGB1 nuclear activities. Nonetheless the weak interaction of HMGB1 with DNA and/or protein partners has also been a major limitation for investigating HMGB1 subnuclear localisation and for the identification of HMGB1 containing complexes by conventional biochemical approaches. In the present study, FRAP experiments demonstrated that DsRed-mediated oligomerization strongly reduces HMGB1 mobility due to an increased affinity for cellular chromatin. Moreover, oligomerized DsRed-HMGB1 exhibited a higher affinity for supercoiled DNA in vitro compared to its monomeric counterpart. These results indicate that DsRed-meditated oligomerization is prone to stabilize labile interactions involving HMGB1 both in vivo and in vitro.

journal_name

Biochimie

journal_title

Biochimie

authors

Messmer M,Klein C,Boniface R,Gnädig NF,Lecerf M,Barnay-Verdier S,Maréchal V

doi

10.1016/j.biochi.2012.11.001

subject

Has Abstract

pub_date

2013-04-01 00:00:00

pages

962-6

issue

4

eissn

0300-9084

issn

1638-6183

pii

S0300-9084(12)00444-0

journal_volume

95

pub_type

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